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Protein

Arylamine N-acetyltransferase

Gene

nat

Organism
Mycobacterium smegmatis
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of the acetyl group from acetyl coenzyme A to the free amino group of arylamines and hydrazines. Substrates include isoniazid, anisidine, and 4-aminoveratrole, and to a much lesser extent, p-aminobenzoic acid.2 Publications

Catalytic activityi

Acetyl-CoA + an arylamine = CoA + an N-acetylarylamine.2 Publications

Kineticsi

  1. KM=25 µM for isoniazid1 Publication
  2. KM=300 µM for anisidine1 Publication
  3. KM=650 µM for 4-aminoveratrole1 Publication
  4. KM=87 µM for isoniazid1 Publication
  5. KM=245 µM for 4-anisidine1 Publication
  6. KM=1.42 mM for 4-aminoveratrole1 Publication
  1. Vmax=63 nmol/min/mg enzyme with isoniazid as substrate1 Publication
  2. Vmax=4.8 nmol/min/mg enzyme with anisidine as substrate1 Publication
  3. Vmax=16.2 nmol/min/mg enzyme with 4-aminoveratrole as substrate1 Publication
  4. Vmax=115 nmol/min/mg enzyme with isoniazid as substrate1 Publication
  5. Vmax=114 nmol/min/mg enzyme with 4-anisidine as substrate1 Publication
  6. Vmax=6.5 µmol/min/mg enzyme with 4-aminoveratrole as substrate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei70 – 701Acyl-thioester intermediate2 Publications
Active sitei110 – 11012 Publications
Active sitei127 – 12712 Publications

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.3.1.5. 3512.

Names & Taxonomyi

Protein namesi
Recommended name:
Arylamine N-acetyltransferase1 Publication (EC:2.3.1.52 Publications)
Short name:
NAT1 Publication
Gene namesi
Name:nat1 Publication
OrganismiMycobacterium smegmatis
Taxonomic identifieri1772 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi70 – 701C → A, S or Q: Loss of activity. 1 Publication
Mutagenesisi110 – 1101H → A, R or W: Loss of activity. 1 Publication
Mutagenesisi127 – 1271D → A, N or W: Loss of activity. 1 Publication

Chemistry

ChEMBLiCHEMBL6060.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 275275Arylamine N-acetyltransferasePRO_0000107918Add
BLAST

Interactioni

Subunit structurei

Homodimer and homotetramer.1 Publication

Protein-protein interaction databases

STRINGi246196.MSMEG_0306.

Chemistry

BindingDBiO86309.

Structurei

Secondary structure

1
275
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 117Combined sources
Helixi22 – 3514Combined sources
Helixi41 – 444Combined sources
Helixi54 – 618Combined sources
Turni62 – 643Combined sources
Helixi70 – 8415Combined sources
Beta strandi87 – 959Combined sources
Beta strandi108 – 1169Combined sources
Beta strandi120 – 1223Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi139 – 1413Combined sources
Beta strandi143 – 1475Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi154 – 1596Combined sources
Beta strandi162 – 1698Combined sources
Beta strandi172 – 1798Combined sources
Helixi186 – 19813Combined sources
Helixi203 – 2064Combined sources
Beta strandi209 – 2135Combined sources
Beta strandi215 – 2228Combined sources
Beta strandi225 – 2306Combined sources
Beta strandi233 – 2419Combined sources
Helixi242 – 25110Combined sources
Helixi257 – 2604Combined sources
Helixi265 – 2717Combined sources
Turni272 – 2743Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GX3X-ray1.70A/B/C/D1-275[»]
1W5RX-ray1.45A/B1-275[»]
1W6FX-ray2.10A/B/C/D1-275[»]
ProteinModelPortaliO86309.
SMRiO86309. Positions 1-275.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO86309.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108MUX. Bacteria.
COG2162. LUCA.

Family and domain databases

InterProiIPR001447. Arylamine_N-AcTrfase.
[Graphical view]
PANTHERiPTHR11786. PTHR11786. 1 hit.
PfamiPF00797. Acetyltransf_2. 1 hit.
[Graphical view]
PRINTSiPR01543. ANATRNSFRASE.

Sequencei

Sequence statusi: Complete.

O86309-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMDLGGYLT RIGLDGRPRP DLGTLHAIVA AHNRSIPFEN LDPLLGIPVA
60 70 80 90 100
DLSAEALFAK LVDRRRGGYC YEHNGLLGYV LEELGFEVER LSGRVVWMRA
110 120 130 140 150
DDAPLPAQTH NVLSVAVPGA DGRYLVDVGF GGQTLTSPIR LEAGPVQQTR
160 170 180 190 200
HEPYRLTRHG DDHTLAAQVR GEWQPLYTFT TEPRPRIDLE VGSWYVSTHP
210 220 230 240 250
GSHFVTGLTV AVVTDDARYN LRGRNLAVHR SGATEHIRFD SAAQVLDAIV
260 270
NRFGIDLGDL AGRDVQARVA EVLDT
Length:275
Mass (Da):30,174
Last modified:December 1, 2000 - v3
Checksum:iC35800574905D3B9
GO

Sequence cautioni

The sequence CAA07100.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006588 Genomic DNA. Translation: CAA07100.2. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006588 Genomic DNA. Translation: CAA07100.2. Different initiation.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GX3X-ray1.70A/B/C/D1-275[»]
1W5RX-ray1.45A/B1-275[»]
1W6FX-ray2.10A/B/C/D1-275[»]
ProteinModelPortaliO86309.
SMRiO86309. Positions 1-275.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEG_0306.

Chemistry

BindingDBiO86309.
ChEMBLiCHEMBL6060.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108MUX. Bacteria.
COG2162. LUCA.

Enzyme and pathway databases

BRENDAi2.3.1.5. 3512.

Miscellaneous databases

EvolutionaryTraceiO86309.

Family and domain databases

InterProiIPR001447. Arylamine_N-AcTrfase.
[Graphical view]
PANTHERiPTHR11786. PTHR11786. 1 hit.
PfamiPF00797. Acetyltransf_2. 1 hit.
[Graphical view]
PRINTSiPR01543. ANATRNSFRASE.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and characterization of arylamine N-acetyltransferase genes from Mycobacterium smegmatis and Mycobacterium tuberculosis: increased expression results in isoniazid resistance."
    Payton M.A., Auty R., Delgoda R.T., Everitt M., Sim E.
    J. Bacteriol. 181:1343-1347(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  2. "The structure of arylamine N-acetyltransferase from Mycobacterium smegmatis -- an enzyme which inactivates the anti-tubercular drug, isoniazid."
    Sandy J., Mushtaq A., Kawamura A., Sinclair J., Sim E., Noble M.E.M.
    J. Mol. Biol. 318:1071-1083(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE.
  3. "Investigation of the catalytic triad of arylamine N-acetyltransferases: essential residues required for acetyl transfer to arylamines."
    Sandy J., Mushtaq A., Holton S.J., Schartau P., Noble M.E.M., Sim E.
    Biochem. J. 390:115-123(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF WILD-TYPE IN COMPLEX WITH ISONIAZID AND OF MUTANT GLN-70, MUTAGENESIS OF CYS-70; HIS-110 AND ASP-127, ACTIVE SITE.

Entry informationi

Entry nameiNAT_MYCSM
AccessioniPrimary (citable) accession number: O86309
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: January 20, 2016
This is version 86 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.